Volume 8, Issue 2 (2017)
JMBS 2017, 8(2): 105-117 |
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Salehzadeh A, Arasteh A. Effect of environmental factors on aggregation and fibrillation of kappa casein. JMBS 2017; 8 (2) :105-117
URL: http://biot.modares.ac.ir/article-22-821-en.html
URL: http://biot.modares.ac.ir/article-22-821-en.html
Abstract: (7186 Views)
Aim and Background: Amylloid fibrils are filamentus protein aggregates derived from various proteins and peptides. They can be distinguished from other type of features according to their appear shape and electron microscope images, also by dye binding methods, which can indicate induced cross beta structures. Amyloid fibrils are correlated to creating general disease, amyloidosis. Disease such Alzheimer, Parkinson, diabetes type II, and others disease which in each of them, the special kind of protein subjected to form amyloid or amyloid like fibrils. A variety of proteins which they are not converted to amyloid fibrils invivo, can be transform to amyloids in special unstabilizing conditions.
Materials and Methods: Congored spectrophotometric method, ThT fluorescence and CD Data was used for fibril formation assay and Transmission Electron microscopy was used for final affirmation of fibrils.
Results: results shows that maximum amyloid formation was in 5 mg.ml-1 protein concentration, 50 ºC and 7.4 buffer pH.
Conclusion:
With the new approach obtained from the kappa casein, amyloid fibers can be introduced as new nanomaterials, Thus the results, given the diverse applications of nanomaterials, can affirm process optimization of amyloid production from accessible and inexpensive protein in milk.
Materials and Methods: Congored spectrophotometric method, ThT fluorescence and CD Data was used for fibril formation assay and Transmission Electron microscopy was used for final affirmation of fibrils.
Results: results shows that maximum amyloid formation was in 5 mg.ml-1 protein concentration, 50 ºC and 7.4 buffer pH.
Conclusion:
With the new approach obtained from the kappa casein, amyloid fibers can be introduced as new nanomaterials, Thus the results, given the diverse applications of nanomaterials, can affirm process optimization of amyloid production from accessible and inexpensive protein in milk.
Article Type: Research Paper |
Subject:
Agricultural Biotechnology
Received: 2016/02/22 | Accepted: 2017/09/23 | Published: 2018/01/27
Received: 2016/02/22 | Accepted: 2017/09/23 | Published: 2018/01/27
References
1. Stefani,M.,Dobson,C.M.(2003)Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution.J.of Mol.Med.81,678-699
2. Chi,E. Y.,Krishnan, S.,Randolph, T.W., andCarpenter,J., F. (2003)Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation.Pharm.Res.20, 1325-1336.
3. Fink,A.(1998) Protein aggregation: folding aggregates, inclusion bodies and amyloid.Folding and design.3,9-23
4. Murzin,A.G.,Brenner,S.E.,Hubbard,T., andChothia, C. (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures.J.Mol.Biol.247,536-540
5. Wang,W.,Nema,S., andTeagarden,D.(2010)Protein aggregationPathways and influencing factors.Int.j.of pharm.390,89-99.
6. Ohnishi, S., and Takano, K. (2004) Amyloid fibrils from the viewpoint of protein folding.Cell Mol Life Sci 61,511-524
7. Fändrich,M. (2007)On the structural definition of amyloid fibrils and other polypeptide aggregates.Cell Mol. Life Sci.64,2066-2078
8. Kunz, C., Lönnerdal,B.(1990) Human-milk proteins: analysis of casein and casein subunits by anion-exchange chromatography, gel electrophoresis, and specific staining methods.Am. J. Clin. Nutr.51, 37-46
9. Holt, C., Carver, J.A., Ecroyd, H., and Thorn,D.C. (2013)Invited review: Caseins and the casein micelle: Their biological functions, structures, and behavior in foods.J. Dairy Sci.96,6127-6146
10. Nagy, K., Váró, G., and Szalontai, B. (2012) κ-Casein terminates casein micelle build-up by its “soft” secondary structure. Eur. Biophys. J.41,959-968
11. Sokolovski, M., Sheynis, T., Kolusheva, S., and Jelinek,R.(2008) Membrane interactions and lipid binding of casein oligomers and early aggregates.Biochim. Biophys. Acta.1778,2341-2349.
12. Ecroyd, H., Thorn,D., Liu, Y., and Carver,J.(2010) The dissociated form of kappa-casein is the precursor to its amyloid fibril formation.Biochem. J.429,251-260
13. Thorn, D.C.,Meehan,S.,Sunde, M.,Rekas,A.,Gras,S.L.,MacPhee, C.E.,Dobson,C.M., Wilson, M.R., and Carver,J.A.(2005) Amyloid Fibril Formation by Bovine Milk κ-Casein and Its Inhibition by the Molecular Chaperones αS-and β-Casein. Biochem.44, 17027-17036
14. Carrotta, R., Canale,C., Diaspro,A., Trapani, A., San Biagio,P., and Bulone, D. (2012) Inhibiting effect of α s1-casein on Aβ 1–40 fibrillogenesis.Biochim. Biophys. Acta.1820,124-132
15. toll, V.S., and Blanchard,J.S.(1990) Buffers: Principles and practice.Meth. Enzymol.182,24-38
16. Chiti, F., and Dobson,C.M. (2006)Protein misfolding, functional amyloid, and human disease.Annul.Rev.Biochem.75,333-366.
17. eyashekar, N.S., Sadana,A., andVo-Dinh,T. (2005) Proteinamyloidose misfolding: mechanisms, detection, and pathological implications.Meth.Mol.Biol.300,417-435
18. Dobson,C. (2006)Protein aggregation and its consequences for human disease.ProteinPept. Lett.13,219-227.
19. Scheibel,T.,Parthasarathy,R.,Sawicki, G., Lin, X.M., Jaeger,H., andLindquist,S.L.(2003) Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition.Proc.Natl.Acad.Sci. USA 100,4527-4532.
20. Hamada,D.,Yanagihara,I., andTsumoto,K. (2004)Engineering amyloidogenicity towards the development of nanofibrillar materials.Trends Biotechnol.22,93-97.
21. Collins,S.R.,Douglass,A.,Vale,R.D., and Weissman, J.S. (2004) Mechanism of prion propagation: amyloid growth occurs by monomer addition.PLoS Biol.2,e321
22. Li, J., Uversky,V.N., and Fink,A.L. (2001)Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochem.40,11604-11613
23. Baxa,U.(2008) Structural basis of infectious and non-infectious amyloids, Curr Alzheimer Res.5,308-318
24. Chiti, F., and Dobson,C.M. (2009)Amyloid formation by globular proteins under native conditions.Nat.Chem.Bio.l 5, 15-22
25. Heo, C., Chang,K.A.,Choi, H.S., Kim, H.S., Kim, S., Liew, H., Kim,J.A., Yu, E. , andSuh,Y.H. (2007)Effects of the monomeric, oligomeric, and fibrillar Abeta42 peptides on the proliferation and differentiation of adult neural stem cells from subventricular zone.J.Neurochem,102,493-500.
26. Resende, R., Ferreiro,E.,Pereira, C., and De Oliveira,C.R. (2008)Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1-42: Involvement of endoplasmic reticulum calcium release in oligomer-induced cell death.Neuroscience 155,725-737
27. Shaykhalishahi, H., Taghizadeh,M., Yazdanparast,R., andChang,Y.T. (2010)Anti-amyloidogenic effect of AA3E2 attenuates beta-amyloid induced toxicity in SK-N-MC cells.Chem.Biol.Interact.186,16-23
28. Masuda,M.,Suzuki,N.,Taniguchi, S.,Oikawa, T., Nonaka,T.,Goedert, M., Hasegawa,M. (2006)Small molecule inhibitors of alpha-synuclein filament assembly.Biochem.45,6085-6094
29. Finke, J.M.,Roy,M.,Zimm, B.H., and Jennings,P.A.(2000) Aggregation events occur prior to stable intermediate formation during refolding of interleukin 1.Biochem.39,575-583.
30. Gupta,P.,Hall,C.K.,VoeglerA.C. (1998)Effect of denaturant and protein concentrations upon protein refolding and aggregation: A simple lattice model.Protein Sci.7,2642-2652.
31. Speed,M.A.,King,J.,Wang,D.C. (1997)Polymerization mechanism of polypeptide chain aggregation.Biotechnol. Bioeng.54,333-343.
32. Vermeer,A.P.,andNorde,W.(2000) The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein.Biophys. J.78,394-404.
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